V
Vera Knäuper
Researcher at Cardiff University
Publications - 87
Citations - 10418
Vera Knäuper is an academic researcher from Cardiff University. The author has contributed to research in topics: Matrix metalloproteinase & Collagenase. The author has an hindex of 49, co-authored 86 publications receiving 10091 citations. Previous affiliations of Vera Knäuper include Arthritis Research UK & University of East Anglia.
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Journal ArticleDOI
Biochemical Characterization of Human Collagenase-3
TL;DR: Analysis of the substrate specificity of collagenase-3 revealed that soluble type II collagen was preferentially hydrolyzed, while the enzyme was 5 or 6 times less efficient at cleaving type I or III collagen.
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Cellular Mechanisms for Human Procollagenase-3 (MMP-13) Activation EVIDENCE THAT MT1-MMP (MMP-14) AND GELATINASE A (MMP-2) ARE ABLE TO GENERATE ACTIVE ENZYME
Vera Knäuper,Horst Will,Carlos López-Otín,Bryan D. Smith,Susan J. Atkinson,Heather Stanton,Rosalind M. Hembry,Gillian Murphy +7 more
TL;DR: It is established that progelatinase A can considerably potentiate the activation rate of procollagenase-3 by crude plasma membrane preparations from concanavalin A-stimulated fibroblasts, thus confirming the results using purified progelasinase A and MT1-MMP.
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TNF-α converting enzyme (TACE) is inhibited by TIMP-3
Augustin Amour,Patrick M. Slocombe,Ailsa Webster,Michael J. Butler,C. Graham Knight,Bryan J. Smith,Paul E. Stephens,Chris Shelley,Mike Hutton,Vera Knäuper,Andrew J. P. Docherty,Gillian Murphy +11 more
TL;DR: Results suggest that TIMP‐3, unlike the other TIMPs, may be important in the modulation of pathological events in which TNF‐α secretion is involved.
Journal ArticleDOI
Mechanisms for pro matrix metalloproteinase activation.
Gillian Murphy,Heather Stanton,Susan Cowell,Georgina S. Butler,Vera Knäuper,Susan J. Atkinson,Jelena Gavrilovic +6 more
TL;DR: The regulation of MT‐MMPs themselves becomes critical to the determination of MMP activity, which includes activation, assembly at the cell surfaces as TIMP‐2 complexes and subsequent inactivation by proteolysis or TIMP inhibition.
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The in vitro activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3.
Augustin Amour,C. Graham Knight,Ailsa Webster,Patrick M. Slocombe,Paul E. Stephens,Vera Knäuper,Andrew J. P. Docherty,Gillian Murphy +7 more
TL;DR: TIMP‐1 inhibition of ADAM‐10 could prove useful in distinguishing its activity from that of TACE, which is only inhibited by TIMP‐3, in cell based assays.